Your browser doesn't support javascript.
loading
Meiotic telomere clustering requires actin for its formation and cohesin for its resolution.
Trelles-Sticken, Edgar; Adelfalk, Caroline; Loidl, Josef; Scherthan, Harry.
Afiliação
  • Trelles-Sticken E; Max-Planck-Institute for Molecular Genetics, D-14195 Berlin, Germany.
J Cell Biol ; 170(2): 213-23, 2005 Jul 18.
Article em En | MEDLINE | ID: mdl-16027219
ABSTRACT
In diploid organisms, meiosis reduces the chromosome number by half during the formation of haploid gametes. During meiotic prophase, telomeres transiently cluster at a limited sector of the nuclear envelope (bouquet stage) near the spindle pole body (SPB). Cohesin is a multisubunit complex that contributes to chromosome segregation in meiosis I and II divisions. In yeast meiosis, deficiency for Rec8 cohesin subunit induces telomere clustering to persist, whereas telomere cluster-SPB colocalization is defective. These defects are rescued by expressing the mitotic cohesin Scc1 in rec8delta meiosis, whereas bouquet-stage exit is independent of Cdc5 pololike kinase. An analysis of living Saccharomyces cerevisiae meiocytes revealed highly mobile telomeres from leptotene up to pachytene, with telomeres experiencing an actin- but not microtubule-dependent constraint of mobility during the bouquet stage. Our results suggest that cohesin is required for exit from actin polymerization-dependent telomere clustering and for linking the SPB to the telomere cluster in synaptic meiosis.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Proteínas Fúngicas / Proteínas Nucleares / Actinas / Telômero / Proteínas de Ciclo Celular / Meiose Idioma: En Ano de publicação: 2005 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Proteínas Fúngicas / Proteínas Nucleares / Actinas / Telômero / Proteínas de Ciclo Celular / Meiose Idioma: En Ano de publicação: 2005 Tipo de documento: Article